Pressure assisted partial filling affinity capillary electrophoresis employed for determination of binding constants of human insulin hexamer complexes with serotonin, dopamine, arginine, and phenol
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00501552" target="_blank" >RIV/61388963:_____/19:00501552 - isvavai.cz</a>
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0003267018313655?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0003267018313655?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.aca.2018.11.026" target="_blank" >10.1016/j.aca.2018.11.026</a>
Alternative languages
Result language
angličtina
Original language name
Pressure assisted partial filling affinity capillary electrophoresis employed for determination of binding constants of human insulin hexamer complexes with serotonin, dopamine, arginine, and phenol
Original language description
A new method, pressure assisted partial filling affinity capillary electrophoresis, has been developed to study noncovalent molecular interactions of the hexamer of human insulin (HI) with biologically relevant ligands, basic phenolic neurotransmitters serotonin and dopamine, basic amino acid arginine, and very weakly acidic phenol, in alkaline aqueous media. The apparent binding constants, K-b, of the HI-ligand complexes were determined from the dependence of the effective migration time changes of the above ligands on the variable zone lengths of HI hexamer dissolved in the background electrolyte (BGE) and hydrodynamically introduced into the bare fused silica capillary close to the UV detector. The strong cationic electroosmotic flow (EOF) in alkaline BGEs, 40/40 mM Tris/tricine, pH 8.1, and 25/34 mM NaOH/tricine, pH 8.5, with EOF mobilities 52.0 x 10(-9) and 58.0 x 10(-9) m(2)V(-1)s(-1), respectively, was reduced by the hydrodynamic counter flow induced by external pressure at the outlet capillary end to avoid expulsion of HI zone out of the capillary and to allow HI interaction with both cationic and anionic ligands inside the capillary. The HI hexamer interactions with the above ligands were found to be weak to moderately strong, with K-b values in the range 385-1314 L mol(-1), and decreasing in the order HIphenol > HI-dopamine > HI-serotonin > HI-arginine.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10406 - Analytical chemistry
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Analytica Chimica Acta
ISSN
0003-2670
e-ISSN
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Volume of the periodical
1052
Issue of the periodical within the volume
Apr 4
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
9
Pages from-to
170-178
UT code for WoS article
000456436100019
EID of the result in the Scopus database
2-s2.0-85057043367